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3QWP

Crystal structure of SET and MYND domain containing 3; Zinc finger MYND domain-containing protein 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0000993molecular_functionRNA polymerase II complex binding
A0001162molecular_functionRNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0008168molecular_functionmethyltransferase activity
A0014904biological_processmyotube cell development
A0032259biological_processmethylation
A0033138biological_processpositive regulation of peptidyl-serine phosphorylation
A0042054molecular_functionhistone methyltransferase activity
A0045184biological_processestablishment of protein localization
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0071549biological_processcellular response to dexamethasone stimulus
A0140939molecular_functionhistone H4 methyltransferase activity
A0140954molecular_functionhistone H3K36 dimethyltransferase activity
A0140999molecular_functionhistone H3K4 trimethyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
ACYS62
ACYS65
AHIS83
ACYS87

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS49
ACYS52
ACYS71
ACYS75

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS261
ACYS263
ACYS266
ACYS208

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SAM A 510
ChainResidue
AARG14
AASN16
ATYR124
AGLU130
AASN132
AASN181
ASER202
ALEU203
ALEU204
AASN205
AHIS206
ATYR239
ATYR257
APHE259
AHOH491
AHOH497
AHOH512
AHOH564
AHOH567
AHOH629
AHOH679
AGOL3001

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 3001
ChainResidue
AASN181
ASER182
APHE183
ASER202
AILE237
ATYR239
ATYR257
ASAM510
AHOH518
AHOH751
AGOL3004

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 3004
ChainResidue
ASER182
APHE183
ATHR184
AHOH553
AHOH591
AGOL3001

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 3005
ChainResidue
AGLN191
ALYS297
AASP332
AASP336
ATYR358
AGLN372
ALYS375

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 3006
ChainResidue
APHE151
AGLN152
AILE159
AGLN160
AHOH724

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 3007
ChainResidue
AARG140
AILE179
AGLN256
AHOH640

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 3008
ChainResidue
AASP82
APHE110
AASP114
AGLU142
AHOH582
AHOH685
AHOH876

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 3009
ChainResidue
ACYS238
ALEU240
AMET242
AHIS366
AHOH494
AHOH591
AGOL3010

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 3010
ChainResidue
AILE214
AVAL215
AHIS366
APRO367
AVAL368
AHOH520
AHOH535
AHOH553
AGOL3009

Functional Information from PROSITE/UniProt
site_idPS01360
Number of Residues39
DetailsZF_MYND_1 Zinc finger MYND-type signature. Cdr..Cllgkeklmr........CsqCrvakYCsakCqkkawpd..Hkre.C
ChainResidueDetails
ACYS49-CYS87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS49-CYS87

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.12
ChainResidueDetails
AARG14
AASN205

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS49
ACYS52
ACYS62
ACYS65
ACYS71
ACYS75
AHIS83
ACYS87

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|Ref.12
ChainResidueDetails
ATYR124
AASN132
AASN181
ATYR239
APHE259

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR22

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PDB entries from 2024-07-24

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